Sandbox Reserved 1724: Difference between revisions
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–{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | –{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Vitamin K Epoxide Reductase== | ==Vitamin K Epoxide Reductase== | ||
<StructureSection load='1stp' size='340' side='right' caption='Overall Structure of Vitamin K Epoxide Reductase' scene='90/904329/Vkoroverallblue/ | <StructureSection load='1stp' size='340' side='right' caption='Overall Structure of Vitamin K Epoxide Reductase' scene='90/904329/Vkoroverallblue/6'> | ||
== Introduction == | == Introduction == | ||
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=== Active Site === | === Active Site === | ||
VKOR uses two catalytic amino acids, <scene name='90/904329/Kohhbond/3'> | VKOR uses two catalytic amino acids, <scene name='90/904329/Kohhbond/3'>Tyr139 and Asn80</scene> to stabilize vitamin K in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket <ref name="Liu">PMID:33154105</ref>. | ||
Other than the two previously mentioned hydrogen bonds (Tyr139 and Asn80), vitamin K is also bound via hydrophobic interactions within the binding pocket of VKOR. Hydrophobic residues of VKOR such as <scene name='90/904329/Kohydroaa/4'>Phe83, Phe87, Tyr88</scene>, form a hydrophobic tunnel within the binding pocket <ref name="Liu">PMID:33154105</ref>. | Other than the two previously mentioned hydrogen bonds (Tyr139 and Asn80), vitamin K is also bound via hydrophobic interactions within the binding pocket of VKOR. Hydrophobic residues of VKOR such as <scene name='90/904329/Kohydroaa/4'>Phe83, Phe87, Tyr88</scene>, form a hydrophobic tunnel within the binding pocket <ref name="Liu">PMID:33154105</ref>. | ||
